DEAH-box helicase 15 (DHX15)

DEAH-box helicase 15 (DHX15) is an ATP-dependent RNA helicase and pre-mRNA splicing factor encoded by the DHX15 gene. It is part of the DEAH/RHA-box family of RNA helicases, defined by tandem RecA-like domains and a conserved DEAH (Asp-Glu-Ala-His) signature[6][5][7]. DHX15 catalyzes RNA duplex unwinding by hydrolyzing ATP and remodels ribonucleoprotein complexes, functioning in spliceosome disassembly, ribosome maturation, and regulating RNA-protein interactions critical for proper gene expression[1][2]. DHX15’s enzymatic activity and substrate specificity are tightly regulated via recruitment by adapter proteins, most notably G-patch domain-containing proteins, which stabilize its conformation and boost its ATPase and helicase activities[1][4]. Beyond RNA processing, DHX15 plays a key role in innate immune signaling, acting as a cofactor for pattern-recognition receptors (such as NLRP6 and RIG-I), where it binds viral double-stranded RNA and triggers immune cascades, including inflammasome assembly and interferon production[3]. Abnormal regulation or expression of DHX15 is associated with cancer (e.g., T-cell acute lymphoblastic leukemia via effects on RNA splicing and activation of oncogenic pathways)[6], and it can serve as a host factor exploited by viruses for genomic RNA packaging and replication[4]. Due to its broad and essential cellular roles, DHX15 is considered a potential target for both cancer therapy and antiviral strategies, but its inhibition poses significant safety and selectivity challenges.

Other names

ATP-dependent RNA helicase DHX15DBP1DDX15PRP43PrPp43phPrp43PRPF43DEAH (Asp-Glu-Ala-His) box helicase 15Splicing factor Prp43DEAD/H box-15RNA helicase 2

ATP-dependent unwinding and remodeling of RNA and RNA-protein complexes, facilitated by interaction with G-patch cofactors[1][2][4]. Recruitment by cofactors (e.g., G-patch proteins, pattern recognition receptors) modulates DHX15 cellular localization and activity[2][3][4].